RNH1_HUMAN
ID RNH1_HUMAN Reviewed; 286 AA.
AC O60930; B3KQU4; O60523; O60857; Q57Z93; Q5U0C1; Q6FHD4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Ribonuclease H1;
DE Short=RNase H1;
DE EC=3.1.26.4;
DE AltName: Full=Ribonuclease H type II;
GN Name=RNASEH1; Synonyms=RNH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-4.
RX PubMed=9799596; DOI=10.1006/geno.1998.5497;
RA Cerritelli S.M., Crouch R.J.;
RT "Cloning, expression, and mapping of ribonucleases H of human and mouse
RT related to bacterial RNase HI.";
RL Genomics 53:300-307(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9512096; DOI=10.1089/oli.1.1998.8.53;
RA Wu H., Lima W.F., Crooke S.T.;
RT "Molecular cloning and expression of cDNA for human RNase H.";
RL Antisense Nucleic Acid Drug Dev. 8:53-61(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9894807; DOI=10.1515/bchm.1998.379.12.1407;
RA Frank P., Braunshofer-Reiter C., Poltl A., Holzmann K.;
RT "Cloning, subcellular localization and functional expression of human RNase
RT HII.";
RL Biol. Chem. 379:1407-1412(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-4.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP CHARACTERIZATION.
RX PubMed=10497183; DOI=10.1074/jbc.274.40.28270;
RA Wu H., Lima W.F., Crooke S.T.;
RT "Properties of cloned and expressed human RNase H1.";
RL J. Biol. Chem. 274:28270-28278(1999).
RN [11]
RP FUNCTION.
RX PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026;
RA Skourti-Stathaki K., Proudfoot N.J., Gromak N.;
RT "Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause
RT sites to promote Xrn2-dependent termination.";
RL Mol. Cell 42:794-805(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INVOLVEMENT IN PEOB2, VARIANTS PEOB2 ILE-142 AND VAL-185, AND
RP CHARACTERIZATION OF VARIANTS PEOB2 ILE-142 AND VAL-185.
RX PubMed=26094573; DOI=10.1016/j.ajhg.2015.05.013;
RA Reyes A., Melchionda L., Nasca A., Carrara F., Lamantea E., Zanolini A.,
RA Lamperti C., Fang M., Zhang J., Ronchi D., Bonato S., Fagiolari G.,
RA Moggio M., Ghezzi D., Zeviani M.;
RT "RNASEH1 mutations impair mtDNA replication and cause adult-onset
RT mitochondrial encephalomyopathy.";
RL Am. J. Hum. Genet. 97:186-193(2015).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II)
CC transcription termination by degrading R-loop RNA-DNA hybrid formation
CC at G-rich pause sites located downstream of the poly(A) site and behind
CC the elongating RNAp II (PubMed:21700224). {ECO:0000269|PubMed:10497183,
CC ECO:0000269|PubMed:21700224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC regulatory site, or after substrate binding.;
CC -!- ACTIVITY REGULATION: In the presence of magnesium, manganese is
CC inhibitory.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- INTERACTION:
CC O60930; Q12797-6: ASPH; NbExp=3; IntAct=EBI-2372399, EBI-12092171;
CC O60930; P50402: EMD; NbExp=3; IntAct=EBI-2372399, EBI-489887;
CC O60930; Q92520: FAM3C; NbExp=3; IntAct=EBI-2372399, EBI-2876774;
CC O60930; P62166: NCS1; NbExp=3; IntAct=EBI-2372399, EBI-746987;
CC O60930; Q8IXM6: NRM; NbExp=3; IntAct=EBI-2372399, EBI-10262547;
CC O60930; P17152: TMEM11; NbExp=3; IntAct=EBI-2372399, EBI-723946;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA
CC deletions, autosomal recessive 2 (PEOB2) [MIM:616479]: A form of
CC progressive external ophthalmoplegia, a mitochondrial myopathy
CC characterized by progressive paralysis of the levator palpebrae,
CC orbicularis oculi, and extraocular muscles. PEOB2 patients manifest
CC exercise intolerance, muscle weakness, and signs and symptoms of
CC spinocerebellar ataxia, such as impaired gait and dysarthria. Some
CC patients may have respiratory insufficiency.
CC {ECO:0000269|PubMed:26094573}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=RNase H entry;
CC URL="https://en.wikipedia.org/wiki/RNase_H";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF048995; AAC78564.1; -; mRNA.
DR EMBL; AF048994; AAC78563.1; -; mRNA.
DR EMBL; AF039652; AAC09261.1; -; mRNA.
DR EMBL; AJ224117; CAA11835.1; -; mRNA.
DR EMBL; CR541820; CAG46619.1; -; mRNA.
DR EMBL; BT019670; AAV38476.1; -; mRNA.
DR EMBL; AK075490; BAG52156.1; -; mRNA.
DR EMBL; AC108488; AAX82026.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01061.1; -; Genomic_DNA.
DR EMBL; BC002973; AAH02973.1; -; mRNA.
DR CCDS; CCDS1647.1; -.
DR RefSeq; NP_002927.2; NM_002936.4.
DR PDB; 2QK9; X-ray; 2.55 A; A=136-286.
DR PDB; 2QKB; X-ray; 2.40 A; A/B=136-286.
DR PDB; 2QKK; X-ray; 3.20 A; A/B/E/F/I/J/M/N/R/S/W=136-286.
DR PDB; 3BSU; X-ray; 2.10 A; A/B/C/F/G/H=27-76.
DR PDB; 6VRD; X-ray; 1.30 A; A=1-286.
DR PDBsum; 2QK9; -.
DR PDBsum; 2QKB; -.
DR PDBsum; 2QKK; -.
DR PDBsum; 3BSU; -.
DR PDBsum; 6VRD; -.
DR AlphaFoldDB; O60930; -.
DR SMR; O60930; -.
DR BioGRID; 128882; 49.
DR IntAct; O60930; 16.
DR MINT; O60930; -.
DR STRING; 9606.ENSP00000313350; -.
DR BindingDB; O60930; -.
DR ChEMBL; CHEMBL5893; -.
DR iPTMnet; O60930; -.
DR PhosphoSitePlus; O60930; -.
DR BioMuta; RNASEH1; -.
DR EPD; O60930; -.
DR jPOST; O60930; -.
DR MassIVE; O60930; -.
DR MaxQB; O60930; -.
DR PaxDb; O60930; -.
DR PeptideAtlas; O60930; -.
DR PRIDE; O60930; -.
DR ProteomicsDB; 49675; -.
DR Antibodypedia; 35292; 119 antibodies from 24 providers.
DR DNASU; 246243; -.
DR Ensembl; ENST00000315212.4; ENSP00000313350.3; ENSG00000171865.10.
DR GeneID; 246243; -.
DR KEGG; hsa:246243; -.
DR MANE-Select; ENST00000315212.4; ENSP00000313350.3; NM_002936.6; NP_002927.2.
DR UCSC; uc002qxt.5; human.
DR CTD; 246243; -.
DR DisGeNET; 246243; -.
DR GeneCards; RNASEH1; -.
DR HGNC; HGNC:18466; RNASEH1.
DR HPA; ENSG00000171865; Low tissue specificity.
DR MalaCards; RNASEH1; -.
DR MIM; 604123; gene.
DR MIM; 616479; phenotype.
DR neXtProt; NX_O60930; -.
DR OpenTargets; ENSG00000171865; -.
DR Orphanet; 329336; Adult-onset chronic progressive external ophthalmoplegia with mitochondrial myopathy.
DR PharmGKB; PA38543; -.
DR VEuPathDB; HostDB:ENSG00000171865; -.
DR eggNOG; KOG3752; Eukaryota.
DR GeneTree; ENSGT00390000003466; -.
DR HOGENOM; CLU_030894_0_2_1; -.
DR InParanoid; O60930; -.
DR OMA; ELWYGLY; -.
DR OrthoDB; 1434144at2759; -.
DR PhylomeDB; O60930; -.
DR TreeFam; TF313356; -.
DR BRENDA; 3.1.26.4; 2681.
DR PathwayCommons; O60930; -.
DR SignaLink; O60930; -.
DR BioGRID-ORCS; 246243; 51 hits in 1075 CRISPR screens.
DR ChiTaRS; RNASEH1; human.
DR EvolutionaryTrace; O60930; -.
DR GeneWiki; RNASEH1; -.
DR GenomeRNAi; 246243; -.
DR Pharos; O60930; Tchem.
DR PRO; PR:O60930; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O60930; protein.
DR Bgee; ENSG00000171865; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; O60930; baseline and differential.
DR Genevisible; O60930; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; TAS:ProtInc.
DR GO; GO:0004540; F:ribonuclease activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.970.10; -; 1.
DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR InterPro; IPR017067; RNase_H1_euk.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01693; Cauli_VI; 1.
DR Pfam; PF00075; RNase_H; 1.
DR PIRSF; PIRSF036852; Ribonuclease_H1_euk; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55658; SSF55658; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Primary mitochondrial disease;
KW Progressive external ophthalmoplegia; Reference proteome.
FT CHAIN 1..286
FT /note="Ribonuclease H1"
FT /id="PRO_0000195433"
FT DOMAIN 136..282
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT REGION 101..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT VARIANT 4
FT /note="L -> F (in dbSNP:rs1136545)"
FT /evidence="ECO:0000269|PubMed:9799596, ECO:0000269|Ref.5"
FT /id="VAR_023469"
FT VARIANT 142
FT /note="V -> I (in PEOB2; has partial residual endonuclease
FT activity; dbSNP:rs766294940)"
FT /evidence="ECO:0000269|PubMed:26094573"
FT /id="VAR_074561"
FT VARIANT 185
FT /note="A -> V (in PEOB2; has partial residual endonuclease
FT activity; dbSNP:rs1057517675)"
FT /evidence="ECO:0000269|PubMed:26094573"
FT /id="VAR_074562"
FT CONFLICT 24
FT /note="G -> R (in Ref. 5; AAV38476)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="R -> K (in Ref. 4; CAG46619)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="W -> R (in Ref. 5; AAV38476)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="Q -> R (in Ref. 3; CAA11835)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="M -> I (in Ref. 4; CAG46619)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="Q -> R (in Ref. 3; CAA11835)"
FT /evidence="ECO:0000305"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:3BSU"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3BSU"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:3BSU"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3BSU"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:3BSU"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:6VRD"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6VRD"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:6VRD"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:6VRD"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2QKB"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6VRD"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2QKK"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:6VRD"
SQ SEQUENCE 286 AA; 32064 MW; 400FE04E7E85CA6A CRC64;
MSWLLFLAHR VALAALPCRR GSRGFGMFYA VRRGRKTGVF LTWNECRAQV DRFPAARFKK
FATEDEAWAF VRKSASPEVS EGHENQHGQE SEAKASKRLR EPLDGDGHES AEPYAKHMKP
SVEPAPPVSR DTFSYMGDFV VVYTDGCCSS NGRRRPRAGI GVYWGPGHPL NVGIRLPGRQ
TNQRAEIHAA CKAIEQAKTQ NINKLVLYTD SMFTINGITN WVQGWKKNGW KTSAGKEVIN
KEDFVALERL TQGMDIQWMH VPGHSGFIGN EEADRLAREG AKQSED
